ID A0A194PGL6_PAPXU Unreviewed; 990 AA.
AC A0A194PGL6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Hypoxia up-regulated protein 1 {ECO:0000256|ARBA:ARBA00040503};
GN ORFNames=RR46_13668 {ECO:0000313|EMBL:KPI92447.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI92447.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI92447.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI92447.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI92447.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- FUNCTION: Has a pivotal role in cytoprotective cellular mechanisms
CC triggered by oxygen deprivation. May play a role as a molecular
CC chaperone and participate in protein folding.
CC {ECO:0000256|ARBA:ARBA00037692}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR EMBL; KQ459604; KPI92447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194PGL6; -.
DR STRING; 66420.A0A194PGL6; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10230; HYOU1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR PANTHER; PTHR45639:SF3; HYPOXIA UP-REGULATED PROTEIN 1; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053268}.
FT REGION 654..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 990 AA; 111488 MW; CA80864850908B01 CRC64;
MDISNTRGTA DALPAFEVVS SGVNNVLLGN WGSECDRVRV DVRRASYVEL RRAICARADA
DPKGTLHNCR DRGQTTRRTS LTRPSTIRSI FRWAANVCVL AYIRRLVISI DLGSEWMKIG
IVSPGVPMEI VLNKESKRKT PAVVAFRDGV RTFGEDAVNV GVRFPKNTYK FFLDLLGKSF
DHPLVKAYKE RFPYYDLVAS DRGTPIFVHD ENTKFTPEEL VAQLLAKAKE FAEISHGQPI
SECVITVPGY FNQAERRALK DAAALAGLNV LQLINDYTAI GINYGIFRRK EINETAWYTL
FYDMGAVSTK AALVEYKTVK IKEKGYVETV PQLQVIGVGF DRTLGGFEMT LRLREHLIKA
WLANGGGDVR ASPRAMEKLL REAERLKIVL SANTEHYAQI ENLLDDKDFK VLVTRAEFEE
LCSDLWSRVS GVIQRAVASA AGSGEGAKLV LAGGAARAPA VHEALRKVVG HEPARSINAD
EAATMGAVYR AASLATGYKV APLNVRDAVL LPIQVVFTRN VDGNEKLIRR TLFGPMNPYP
QKKVITFNKH TDDFSFNVNY AELDHIPSTE LKYIGSLNLS QVILSGVSEA LAKHTGDNVE
HKGIKAHFNM DDSGILNLVN VEFVAEKTVT EEDNDKDSTL SKIGSTISKL FSSDSETLEK
VEEKAEDKPK ESEKNETKAN ETTTEKQNAT ETESKPKPKV VVLKEPIKNE EQILNLQPLS
QDQFKESKNK IKELNMIDRK RVERESALNN LEAFVVDAQL KIDMDEYAEC GTQEQIEEIK
KLCSETSEWL YDEGYEADTE TYESKLALLR EKTNPIFYKN WEHRERPDAV AAIRKMLNSS
QEFLKMAKNL TKDTNSERDV FTDVEIDVLE KKIMETQSWL TKSIEDQNQL KKNEDIKLTV
DSIREKMSNL DREVKYLVNK MKIWRPKKPV KKDSDNKTET VIENEKEATP DTADRAEKTE
KPEVLPEQKE DTGGEETLQI SDENPEHSEL
//